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2,3-dihydroxybenzoate + O2
?
2,4-dihydroxybenzoate + O2
?
2,5-dihydroxybenzoate + O2
?
2,6-dihydroxybenzoate + O2
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
3,4-dihydroxybenzoate + O2
?
3,4-dihydroxybenzoate + O2
beta-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
3,4-dihydroxymandelic acid + O2
?
3,4-dihydroxyphenylacetate + O2
?
3,4-dihydroxyphenylalanine + O2
?
Nocardia erythropolis
-
at 10.7% the rate of protocatechuic acid oxidation
-
-
?
3,4-dihydroxyphenylpropionic acid + O2
?
-
-
-
-
-
3,5-dihydroxybenzoate + O2
?
3-(3,4-dihydroxyphenyl)propionate + O2
?
-
protocatechuate 3,4-dioxygenase II
-
-
?
3-methylcatechol + O2
2-methylmuconate
4-cresol + O2
?
-
-
-
-
?
4-hydroxybenzoic acid + O2
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
4-methylcatechol + O2
?
-
-
-
-
?
4-sulfocatechol + O2
3-sulfomuconate
5-fluoro-protocatechuic acid + O2
5-fluoro-3-carboxy-cis,cis-muconate
-
at 2.1% the rate of protocatechuic acid oxidation
-
?
6-chloro-protocatechuate + O2
6-chloro-3-carboxy-cis,cis-muconate
-
at 4.3% the rate of protocatechuic acid oxidation
-
?
catechin + O2
?
-
-
-
-
?
catechol + O2
cis,cis-muconate
protocatechuate + O2
3-carboxy-cis,cis-muconate
protocatechuate + O2
beta-carboxy-cis-cis-muconate
protocatechuic acid + O2
3-carboxy-cis,cis-muconic acid
-
-
-
-
?
trans-3,4-dihydroxycinnamate + O2
?
additional information
?
-
2,3-dihydroxybenzoate + O2

?
I0DHJ0 AND I0DHJ1
23.6% activity compared to 3,4-dihydroxybenzoate
-
-
?
2,3-dihydroxybenzoate + O2
?
I0DHJ0 AND I0DHJ1
23.6% of the activity with protocatechuate for the free enzyme, 149.3% for the calcium alginate-immobilized enzyme, and 119.8% for the glyoxyl agarose-immobilized enzyme
-
-
?
2,4-dihydroxybenzoate + O2

?
I0DHJ0 AND I0DHJ1
43.5% activity compared to 3,4-dihydroxybenzoate
-
-
?
2,4-dihydroxybenzoate + O2
?
I0DHJ0 AND I0DHJ1
43.5% of the activity with protocatechuate for the free enzyme, 96.5% for the calcium alginate-immobilized enzyme, and 65.6% for the glyoxyl agarose-immobilized enzyme
-
-
?
2,5-dihydroxybenzoate + O2

?
I0DHJ0 AND I0DHJ1
33.46% activity compared to 3,4-dihydroxybenzoate
-
-
?
2,5-dihydroxybenzoate + O2
?
I0DHJ0 AND I0DHJ1
33.5% of the activity with protocatechuate for the free enzyme, 158.6% for the calcium alginate-immobilized enzyme, and 72.1% for the glyoxyl agarose-immobilized enzyme
-
-
?
2,6-dihydroxybenzoate + O2

?
I0DHJ0 AND I0DHJ1
30.5% of the activity with protocatechuate for the free enzyme, 90.4% for the calcium alginate-immobilized enzyme, and 36.2% for the glyoxyl agarose-immobilized enzyme
-
-
?
2,6-dihydroxybenzoate + O2
?
I0DHJ0 AND I0DHJ1
30.51% activity compared to 3,4-dihydroxybenzoate
-
-
?
3,4-dihydroxybenzoate + O2

3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
absolute requirement for vicinal hydroxyl groups in the 3- and 4-position
-
ir
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 2-chloro-protocatechuate
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 5-bromo-protocatechuate
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 5-chloro-protocatechuate
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
methylene blue cannot replace O2 as electron acceptor
-
ir
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
Nocardia erythropolis
-
enzyme is active on a wide range of o-dihydroxyphenyl compounds
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with: 3,4-dihydroxyphenylacetic acid
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 3,4-dihydroxymandelic acid
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 4'-methylcatechol
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with: 3,4-dihydroxyphenylacetic acid
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 3,4-dihydroxymandelic acid
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
very low activity with 4'-methylcatechol
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
no other substrate found
-
ir
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
no other substrate found
-
ir
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
i.e. protocatechuate
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
specific for protocatechuate
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
A0A193DXA9 and A0A193DXP2
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
Q0SH27 AND Q0SH26
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
I0DHJ0 AND I0DHJ1
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
I0DHJ0 AND I0DHJ1
best substrate
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
I0DHJ0 AND I0DHJ1
100% activity
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
I0DHJ0 AND I0DHJ1
100% activity
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
I0DHJ0 AND I0DHJ1
-
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
I0DHJ0 AND I0DHJ1
best substrate
-
-
?
3,4-dihydroxybenzoate + O2
3-carboxy-cis,cis-muconate
-
no other substrate found
-
?
3,4-dihydroxybenzoate + O2

?
-
spectroscopic and electronic structure study of the enzyme-substrate complex
-
-
?
3,4-dihydroxybenzoate + O2
?
-
spectroscopic and electronic structure study of the enzyme-substrate complex
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2

?
I0DHJ0 AND I0DHJ1
29.5% of the activity with protocatechuate for the free enzyme, 95.0% for the calcium alginate-immobilized enzyme, and 41.1% for the glyoxyl agarose-immobilized enzyme
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
I0DHJ0 AND I0DHJ1
29.54% ctivity compared to 3,4-dihydroxybenzoate
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
I0DHJ0 AND I0DHJ1
29.54% ctivity compared to 3,4-dihydroxybenzoate
-
-
?
3,4-dihydroxyhydrocinnamic acid + O2
?
I0DHJ0 AND I0DHJ1
29.5% of the activity with protocatechuate for the free enzyme, 95.0% for the calcium alginate-immobilized enzyme, and 41.1% for the glyoxyl agarose-immobilized enzyme
-
-
?
3,4-dihydroxymandelic acid + O2

?
-
protocatechuate 3,4-dioxygenase II
-
-
?
3,4-dihydroxymandelic acid + O2
?
-
protocatechuate 3,4-dioxygenase II
-
-
?
3,4-dihydroxymandelic acid + O2
?
Nocardia erythropolis
-
at 5.4% the rate of protocatechuic acid oxidation
-
-
?
3,4-dihydroxyphenylacetate + O2

?
-
-
-
-
?
3,4-dihydroxyphenylacetate + O2
?
-
W153V protocatechuate 3,4-dioxygenase I mutant enzyme: 13% activity compared to protocatechuate, wild-type protocatechuate 3,4-dioxygenase I: 2% activity compared to protocatechuate
-
-
-
3,4-dihydroxyphenylacetate + O2
?
-
-
-
-
-
3,4-dihydroxyphenylacetate + O2
?
-
-
-
-
?
3,5-dihydroxybenzoate + O2

?
I0DHJ0 AND I0DHJ1
44.3% of the activity with protocatechuate for the free enzyme, 113.3% for the calcium alginate-immobilized enzyme, and 42.9% for the glyoxyl agarose-immobilized enzyme
-
-
?
3,5-dihydroxybenzoate + O2
?
I0DHJ0 AND I0DHJ1
44.33% activity compared to 3,4-dihydroxybenzoate
-
-
?
3-methylcatechol + O2

2-methylmuconate
-
-
-
?
3-methylcatechol + O2
2-methylmuconate
-
-
-
?
3-methylcatechol + O2
2-methylmuconate
-
at 5% the rate of protocatechuic acid oxidation
-
?
3-methylcatechol + O2
2-methylmuconate
-
-
-
?
3-methylcatechol + O2
2-methylmuconate
-
-
-
?
3-methylcatechol + O2
2-methylmuconate
Nocardia erythropolis
-
at 14.4% the rate of protocatechuic acid oxidation
-
?
3-methylcatechol + O2
2-methylmuconate
-
at 0.4% the rate of protocatechuic acid oxidation
-
?
4-hydroxybenzoic acid + O2

?
I0DHJ0 AND I0DHJ1
-
-
-
?
4-hydroxybenzoic acid + O2
?
I0DHJ0 AND I0DHJ1
-
-
-
?
4-methylcatechol + O2

3-methyl-cis,cis-muconate
-
at very low rates
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
at very low rates
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
at very low rates
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
-
at very low rates
-
?
4-methylcatechol + O2
3-methyl-cis,cis-muconate
Nocardia erythropolis
-
at 3.1% the rate of protocatechuic acid oxidation
-
?
4-sulfocatechol + O2

3-sulfomuconate
-
catalyzed by protocatechuate 3,4-dioxgenase type II only
-
?
4-sulfocatechol + O2
3-sulfomuconate
-
catalyzed by protocatechuate 3,4-dioxgenase type II only
-
?
4-sulfocatechol + O2
3-sulfomuconate
-
catalyzed by protocatechuate 3,4-dioxgenase type II only
-
?
caffeic acid + O2

?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
I0DHJ0 AND I0DHJ1
34.2% of the activity with protocatechuate for the free enzyme, 150% for the calcium alginate-immobilized enzyme, and 97% for the glyoxyl agarose-immobilized enzyme
-
-
?
caffeic acid + O2
?
I0DHJ0 AND I0DHJ1
34.21% activity compared to 3,4-dihydroxybenzoate
-
-
?
caffeic acid + O2
?
I0DHJ0 AND I0DHJ1
34.21% activity compared to 3,4-dihydroxybenzoate
-
-
?
caffeic acid + O2
?
I0DHJ0 AND I0DHJ1
34.2% of the activity with protocatechuate for the free enzyme, 150% for the calcium alginate-immobilized enzyme, and 97% for the glyoxyl agarose-immobilized enzyme
-
-
?
catechol + O2

cis,cis-muconate
-
reaction of EC 1.13.11.1
-
-
?
catechol + O2
cis,cis-muconate
-
reaction of EC 1.13.11.1
-
-
?
catechol + O2

muconate
-
-
-
?
catechol + O2
muconate
-
-
-
?
catechol + O2
muconate
-
at 3% the rate of protocatechuic acid oxidation
-
?
catechol + O2
muconate
-
-
-
-
?
catechol + O2
muconate
-
-
-
?
catechol + O2
muconate
-
-
-
?
catechol + O2
muconate
Nocardia erythropolis
-
at 33.8% the rate of protocatechuic acid oxidation
-
?
catechol + O2
muconate
-
at 0.4% the rate of protocatechuic acid oxidation
-
?
catechol + O2
muconate
-
at 0.4% the rate of protocatechuic acid oxidation
-
?
protocatechuate + O2

3-carboxy-cis,cis-muconate
-
-
-
-
?
protocatechuate + O2
3-carboxy-cis,cis-muconate
-
-
-
-
?
protocatechuate + O2

beta-carboxy-cis-cis-muconate
-
-
-
-
?
protocatechuate + O2
beta-carboxy-cis-cis-muconate
-
-
-
-
?
protocatechuate + O2
beta-carboxy-cis-cis-muconate
-
-
-
-
?
protocatechuate + O2
beta-carboxy-cis-cis-muconate
-
-
-
-
?
pyrogallol + O2

?
-
at 10% the rate of protocatechuic acid oxidation
-
-
?
pyrogallol + O2
?
Nocardia erythropolis
-
at 36% the rate of protocatechuic acid oxidation
-
-
?
pyrogallol + O2
?
-
at 0.4% the rate of protocatechuic acid oxidation
-
-
?
pyrogallol + O2
?
-
at 0.4% the rate of protocatechuic acid oxidation
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
trans-3,4-dihydroxycinnamate + O2

?
-
-
-
-
?
trans-3,4-dihydroxycinnamate + O2
?
-
W153V protocatechuate 3,4-dioxygenase I mutant enzyme: 35% activity compared to protocatechuate, wild-type protocatechuate 3,4-dioxygenase I: 2% activity compared to protocatechuate
-
-
-
trans-3,4-dihydroxycinnamate + O2
?
-
-
-
-
?
vanillic acid + O2

?
I0DHJ0 AND I0DHJ1
-
-
-
?
vanillic acid + O2
?
I0DHJ0 AND I0DHJ1
-
-
-
?
additional information

?
-
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
-
additional information
?
-
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
-
additional information
?
-
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
-
additional information
?
-
benzoate induces expression of protocatechuate 3,4-dioxygenase
-
-
-
additional information
?
-
-
no activity with gentisate
-
-
-
additional information
?
-
-
enzyme involved in last ring fission in naphtalene degradation, intermediates confirm proceeding through protocatechuic acid via ortho-claevage pathway
-
-
-
additional information
?
-
-
the enzyme is active on a wide range of phenyl compounds, in contrast to the high specificity of similar enzymes from other sources
-
-
-
additional information
?
-
-
the enzyme is active on a wide range of phenyl compounds, in contrast to the high specificity of similar enzymes from other sources
-
-
-
additional information
?
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strain KB2 degrades 13 mM 3,4-dihydroxybenzoate, 10 mM benzoic acid and 12 mM phenol within 24 h of incubation
-
-
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additional information
?
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I0DHJ0 AND I0DHJ1
protocatechuate 3,4-dioxygenase from KB2 strain shows activity against various dihydroxybenzoic acids, but highest activity with primary substrate protocatechuate. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate, overview
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-
-
additional information
?
-
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protocatechuate 3,4-dioxygenase from KB2 strain shows activity against various dihydroxybenzoic acids, but highest activity with primary substrate protocatechuate. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate, overview
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-
-
additional information
?
-
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strain KB2 degrades 13 mM 3,4-dihydroxybenzoate, 10 mM benzoic acid and 12 mM phenol within 24 h of incubation
-
-
-
additional information
?
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I0DHJ0 AND I0DHJ1
protocatechuate 3,4-dioxygenase from KB2 strain shows activity against various dihydroxybenzoic acids, but highest activity with primary substrate protocatechuate. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate, overview
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(2E)-3-(3,4-dimethoxyphenyl)-N-hydroxyprop-2-enamide
Q0SH27 AND Q0SH26
over 90% inhibition at 0.2 mM
(2E)-N-hydroxy-3-(4-methoxyphenyl)prop-2-enamide
Q0SH27 AND Q0SH26
over 90% inhibition at 0.2 mM
1,10-phenanthroline
-
0.005 mM, approx. 50% inhibition after 30 min, complete inhibition after 60 min, complete restoration of inactivated enzyme by addition of excess ferric EDTA complex
2,4-dihydroxybenzoic acid
-
competitive inhibition
2,5-Dihydroxybenzoate
-
-
2-(2H-1,3-benzodioxol-5-yl)-N-[(4-fluorophenyl)methyl]-N-hydroxyacetamide
Q0SH27 AND Q0SH26
60% inhibition at 0.2 mM
2-Fluoro-4-hydroxybenzoate
-
-
2-Hydroxyisonicotinic acid N-oxide
2-Hydroxypyridine N-oxide
-
-
3,4-Dihydroxyacetophenone
3,4-dihydroxybenzoate
-
-
3,4-dihydroxycinnamic acid
-
-
3,4-Dihydroxyphenylacetate
-
-
3,4-dihydroxyphenylacetic acid
3,4-Dihydroxyphenylpropionate
-
-
3,5-Dichloro-4-hydroxybenzoate
-
-
3-(3,4-dimethoxyphenyl)-N-hydroxy-N-octylpropanamide
Q0SH27 AND Q0SH26
57% inhibition at 0.2 mM
3-(3,4-dimethoxyphenyl)-N-hydroxypropanamide
Q0SH27 AND Q0SH26
60% inhibition at 0.2 mM
3-Bromo-4-hydroxybenzoate
-
-
3-Chloro-4-hydroxybenzoate
-
-
3-Fluoro-4-hydroxybenzoate
3-hydroxyphenylacetic acid
-
-
3-Nitrophenol
-
0.006 mM, 56% inhibition
4-(dimethylamino)benzaldehyde
-
-
4-Fluoro-3-hydroxybenzoate
4-hydroxyphenylacetic acid
-
-
alpha-chloro-3,4-dihydroxyacetophenone
-
-
Ca2+
Nocardia erythropolis
-
-
Ferrous ammonium sulfate
-
-
Hg2+
Nocardia erythropolis
-
0.1 mM, 45% inhibition
isonicotinic acid N-oxide
-
-
K+
A0A193DXA9 and A0A193DXP2
16.7% residual activity at 1 mM
KF
-
50 mM, 34% inhibition
Mg2+
A0A193DXA9 and A0A193DXP2
50% residual activity at 1 mM
Na2HAsO4
Nocardia erythropolis
-
0.1 mM, 50% inhibition
Nickel ammonium sulfate
-
-
o-Chloranil
-
0.006 mM, 51% inhibition
p-chloromercuribenzoate
-
0.05 mM, 47% inhibition
Pb2+
Nocardia erythropolis
-
-
Protocatechuic acid methyl ester
-
-
2,2'-dipyridyl

I0DHJ0 AND I0DHJ1
activates the enzyme immobilized on calcium alginate, but inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose, at 0.3 mM
2,2'-dipyridyl
I0DHJ0 AND I0DHJ1
87.62% residual activity at 3 mM
2,3-Dihydroxybenzoate

-
-
2,3-Dihydroxybenzoate
-
-
2-Hydroxyisonicotinic acid N-oxide

-
0.000025 mM, 50% inactivation after 10 min, most potent inhibitor
2-Hydroxyisonicotinic acid N-oxide
-
-
3,4-Dihydroxyacetophenone

-
-
3,4-Dihydroxyacetophenone
-
-
3,4-dihydroxyphenylacetic acid

-
0.006 mM, 92% inhibition
3,4-dihydroxyphenylacetic acid
-
-
3,4-dihydroxyphenylacetic acid
-
-
3-Fluoro-4-hydroxybenzoate

-
-
3-Fluoro-4-hydroxybenzoate
-
-
3-hydroxybenzoate

-
-
3-hydroxybenzoate
-
optical titration at 25°C
4-Fluoro-3-hydroxybenzoate

-
-
4-Fluoro-3-hydroxybenzoate
-
-
4-hydroxybenzoate

-
-
4-hydroxybenzoate
-
optical titration at 25°C
4-hydroxymercuribenzoate

-
0.006 mM, 80% inhibition
4-hydroxymercuribenzoate
-
-
4-hydroxymercuribenzoate
-
0.1 mM, complete inhibition
4-methylcatechol

-
0.006 mM, 59% inhibition
4-nitrocatechol

-
0.006 mM, complete inhibition
4-sulfocatechol

-
competitive vs. protocatechuate
4-sulfocatechol
-
competitive vs. protocatechuate
Al3+

-
EDTA salt, 0.01 mM, complete inhibition
Al3+
A0A193DXA9 and A0A193DXP2
23.1% residual activity at 1 mM
Al3+
-
inhibits 66.5% at 3 mM
Al3+
I0DHJ0 AND I0DHJ1
slight inhibition of the glyoxyl agarose-immobilized enzyme
butanol

A0A193DXA9 and A0A193DXP2
about 75% residual activity at 100 mM
butanol
I0DHJ0 AND I0DHJ1
inhibits the activity of the enzyme immobilized on glyoxyl agarose by 23.5% at 0.3 mM
catechol

-
0-006 mM, 63% inhibition
Cd2+

-
inhibits 40% at 3 mM
Co2+

-
inhibits 48.5% at 3 mM
Cu2+

-
inhibits 70% at 3 mM
EDTA

I0DHJ0 AND I0DHJ1
activates the enzyme immobilized on calcium alginate, but inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose, at 0.3 mM
EDTA
I0DHJ0 AND I0DHJ1
18.19% residual activity at 3 mM
ethanol

A0A193DXA9 and A0A193DXP2
about 50% residual activity at 100 mM
ethanol
I0DHJ0 AND I0DHJ1
inhibits the activity of the enzyme immobilized on glyoxyl agarose by 50% at 0.3 mM
Fe3+

-
inhibits 77% at 3 mM
Fe3+
I0DHJ0 AND I0DHJ1
inhibits the free enzyme and the enzyme immobilized on glyoxyl agarose
iodoacetate

Nocardia erythropolis
-
-
iodoacetate
-
5 mM, 20% inhibition
iodoacetate
-
0.1 mM, complete inhibition
methanol

A0A193DXA9 and A0A193DXP2
about 75% residual activity at 100 mM
methanol
I0DHJ0 AND I0DHJ1
inhibits the activity of the enzyme immobilized on calcium alginate by 28% at 0.3 mM
methanol
I0DHJ0 AND I0DHJ1
91.53% residual activity at 200 mM
Mn2+

A0A193DXA9 and A0A193DXP2
45.2% residual activity at 1 mM
Mn2+
-
inhibits 19% at 3 mM
N-ethylmaleimide

Nocardia erythropolis
-
-
N-ethylmaleimide
-
0.1 mM, complete inhibition
Ni2+

-
EDTA salt, 0.01 mM, 72% inhibition
Ni2+
A0A193DXA9 and A0A193DXP2
38.3% residual activity at 1 mM
Ni2+
-
inhibits 17% at 3 mM
Phenanthroline

I0DHJ0 AND I0DHJ1
-
Phenanthroline
I0DHJ0 AND I0DHJ1
69.69% residual activity at 3 mM
Propanol

A0A193DXA9 and A0A193DXP2
about 40% residual activity at 100 mM
Propanol
I0DHJ0 AND I0DHJ1
inhibits the activity of the enzyme immobilized on glyoxyl agarose by 23% at 0.3 mM
Protocatechualdehyde

-
0.006 mM, 54% inhibition
Protocatechualdehyde
-
competitive inhibitor
protocatechuate

-
competitive vs. 4-sulfocatechol
protocatechuate
-
competitive vs. 4-sulfocatechol
Zn2+

-
inhibits 49% at 3 mM
additional information

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not inhibited by iodoacetamide, 5,5'-dithiobis(2-nitrobenzoate), mercaptoethanol, dithiothreitol, glutathione, o-phenanthroline and H2O2
-
additional information
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not inhibited by arsenate, iodoacetate, semicarbazide, N-phenylmaleimide, fluoride or cyanide
-
additional information
Q0SH27 AND Q0SH26
poor inhibition by N-hydroxy-3-(4-methoxyphenyl)propanamide at 0.2 mM
-
additional information
-
poor inhibition by N-hydroxy-3-(4-methoxyphenyl)propanamide at 0.2 mM
-
additional information
I0DHJ0 AND I0DHJ1
protective effect of immobilization on calcium alginate on enzyme activity is observed in the presence of Cd2+, Al3+, and Fe3+ while in the presence of Mn2+ and Zn2+ the inhibitory effect of metals on enzyme activity increases
-
additional information
-
protective effect of immobilization on calcium alginate on enzyme activity is observed in the presence of Cd2+, Al3+, and Fe3+ while in the presence of Mn2+ and Zn2+ the inhibitory effect of metals on enzyme activity increases
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DELTA319-322
-
turnover-number is 4.14fold lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 2.1fold lower than that of the wild-type enzyme
R457S
-
turnover-number is 1333fold lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 2.2fold lower than that of the wild-type enzyme
R142K
-
like wild-type no acticity of mutated protocatechuate 3,4-dioxygenase I with 4-sulfocatechol
R142K/W153V
-
protocatechuate 3,4-dioxygenase I gain of function mutation, mutant enzyme oxidizes 4-sulfocatechol
R153V
-
protocatechuate 3,4-dioxygenase I gain of function mutation, mutant enzyme oxidizes 4-sulfocatechol
Y408F
-
iron is not tightly bound, the Y408F mutant does not reconstitute above half-occupancy and loses color during crystallization attempts. Inhibitors like 4-hydroybenzoate and 3-hydroybenzoate bind more tighly to the mutant enzyme, whereas the substrate protocatechuate binds less tightly.
R133H

-
gain of function mutation confers catechol 1,2-dioxygenase activity
R133H
-
turnover-number is fold 500lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 1.8fold higher than that of the wild-type enzyme
Y408C

-
turnover-number is 523fold lower than that of the wild-type enzyme
Y408C
-
iron is tightly bound. The structure reveals no significant mutation-related changes except in the immediate vicinity of the altered amino acid (rmsd over all atoms = 0.2-0.3 A). The new amino acid does not coordinate to the iron, because the side chain is shorter than that of Tyr. In contrast to the wild-type enzyme, Tyr447 remains bound to the iron, as a result, a monodentate substrate complex is formed between the iron and protocatechuate 04. Protocatechuate does not shift into a chelated orientation. Inhibitors like 4-hydroybenzoate and 3-hydroybenzoate bind more tighly to the mutant enzyme, whereas the substrate protocatechuate binds less tightly.
Y408E

-
turnover-number is 6800fold lower than that of the wild-type enzyme
Y408E
-
iron is tightly bound. The structure reveals no significant mutation-related changes except in the immediate vicinity of the altered amino acid (rmsd over all atoms = 0.2-0.3 A). The new amino acid does not coordinate to the iron, because the side chain is shorter than that of Tyr. In contrast to the wild-type enzyme, Tyr447 remains bound to the iron, as a result, a monodentate substrate complex is formed between the iron and protocatechuate 04. Protocatechuate does not shift into a chelated orientation.
Y408H

-
turnover-number is 9714fold lower than that of the wild-type enzyme, the Km-value for 3,4-dihydroxybenzoate is 10fold lower than that of the wild-type enzyme
Y408H
-
iron is tightly bound. The structure reveals no significant mutation-related changes except in the immediate vicinity of the altered amino acid (rmsd over all atoms = 0.2-0.3 A). The new amino acid does not coordinate to the iron, because the side chain is shorter than that of Tyr. In contrast to the wild-type enzyme, Tyr447 remains bound to the iron, as a result, a monodentate substrate complex is formed between the iron and protocatechuate 04. Protocatechuate does not shift into a chelated orientation. Inhibitors like 4-hydroybenzoate and 3-hydroybenzoate bind more tighly to the mutant enzyme, whereas the substrate protocatechuate binds less tightly.
Y447H

-
greatly reduced rate of protocatechuate oxygenation
Y447H
-
turnover-number is 567fold lower than that of the wild-type enzyme
additional information

-
mutants are constructed so that their pcaG genes contained variations in repeat sequence capable of producing a selectable phenotype following a specific deletion. Deletion frequencies of the various mutations is determined and compared with repair frequencies of three different single-base mutations.
additional information
-
mutants are constructed so that their pcaG genes contained variations in repeat sequence capable of producing a selectable phenotype following a specific deletion. Deletion frequencies of the various mutations is determined and compared with repair frequencies of three different single-base mutations.
-
additional information
-
immobilization of the enzyme, the immobilized extract exhibited higher enzyme activity than the cell-free extract in the presence of trace elements and cations
additional information
I0DHJ0 AND I0DHJ1
immobilization of the enzyme in alginate gel shifts its optimum pH towards high-alkaline pH while immobilization of the enzyme on glyoxyl agarose does not influence pH-profile of the enzyme. Protocatechuate 3,4-dioygenase immobilized in calcium alginate shows increased activity towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate. Slightly lower activity of the enzyme is observed after its immobilization on glyoxyl agarose. Entrapment of the enzyme in alginate gel protects it against chelators and aliphatic alcohols while its immobilization on glyoxyl agarose enhanced enzyme resistance to inactivation by metal ions. Immobilization of dioxygenase in calcium alginate or on glyoxyl agarose results in decrease in the optimum temperature by 5°C and10°C, respectively. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate
additional information
-
immobilization of the enzyme in alginate gel shifts its optimum pH towards high-alkaline pH while immobilization of the enzyme on glyoxyl agarose does not influence pH-profile of the enzyme. Protocatechuate 3,4-dioygenase immobilized in calcium alginate shows increased activity towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate. Slightly lower activity of the enzyme is observed after its immobilization on glyoxyl agarose. Entrapment of the enzyme in alginate gel protects it against chelators and aliphatic alcohols while its immobilization on glyoxyl agarose enhanced enzyme resistance to inactivation by metal ions. Immobilization of dioxygenase in calcium alginate or on glyoxyl agarose results in decrease in the optimum temperature by 5°C and10°C, respectively. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate
additional information
-
immobilization of the enzyme in alginate gel shifts its optimum pH towards high-alkaline pH while immobilization of the enzyme on glyoxyl agarose does not influence pH-profile of the enzyme. Protocatechuate 3,4-dioygenase immobilized in calcium alginate shows increased activity towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate. Slightly lower activity of the enzyme is observed after its immobilization on glyoxyl agarose. Entrapment of the enzyme in alginate gel protects it against chelators and aliphatic alcohols while its immobilization on glyoxyl agarose enhanced enzyme resistance to inactivation by metal ions. Immobilization of dioxygenase in calcium alginate or on glyoxyl agarose results in decrease in the optimum temperature by 5°C and10°C, respectively. Activity of the enzyme immobilized on calcium alginate increases particularly towards 2,5-dihydroxybenzoate, caffeic acid, 2,3-dihydroxybenzoate, and 3,5-dihydroxybenzoate
-
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